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Published online 9 February 2004. doi:10.1083/jcb.200308061
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 164, Number 4, 567-580
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Article

Capping protein binding to actin in yeast

: biochemical mechanism and physiological relevance



Kyoungtae Kim1, Atsuko Yamashita2, Martin A. Wear1, Yuichiro Maéda2, and John A. Cooper1

1 Department of Cell Biology and Physiology, Washington University School of Medicine, St. Louis, MO 63110
2 Laboratory for Structural Biochemistry, RIKEN Harima Institute at SPring-8, Hyogo 679-5148, Japan

Address correspondence to John A. Cooper, Campus Box 8228, 660 S. Euclid Ave., St. Louis, MO 63110. Tel.: (314) 362-3964. Fax: (314) 362-0098. email: jcooper{at}cellbiology.wustl.edu

The mechanism by which capping protein (CP) binds barbed ends of actin filaments is not understood, and the physiological significance of CP binding to actin is not defined. The CP crystal structure suggests that the COOH-terminal regions of the CP {alpha} and ß subunits bind to the barbed end. Using purified recombinant mutant yeast CP, we tested this model. CP lacking both COOH-terminal regions did not bind actin. The {alpha} COOH-terminal region was more important than that of ß. The significance of CP's actin-binding activity in vivo was tested by determining how well CP actin-binding mutants rescued null mutant phenotypes. Rescue correlated well with capping activity, as did localization of CP to actin patches, indicating that capping is a physiological function for CP. Actin filaments of patches appear to be nucleated first, then capped with CP. The binding constants of yeast CP for actin suggest that actin capping in yeast is more dynamic than in vertebrates.

Key Words: cytoskeleton; cell motility; polymerization; assembly; Saccharomyces cerevisiae

A. Yamashita's present address is Dept. of Biochemistry and Molecular Biophysics, Columbia University, Room 513, Black Building, 650 West 168th St., New York, NY 10032.

Abbreviations used in this paper: CP, capping protein; wt, wild type.


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